AI Article Synopsis
- Molecular modeling techniques were used to investigate how oligomeric derivatives of phenols interact with the peroxidase enzyme from Arthromyces ramosus.
- The study found that as the length of these oligomers increases, their affinity for the enzyme also rises, but this leads to the formation of non-productive complexes.
- The stable complex formation inhibits peroxidase activity by blocking the active site from regular substrates, hindering the enzyme's function.
Article Abstract
Molecular modeling techniques were applied to study oligomeric derivatives of phenols, which are produced during peroxidase-catalyzed oxidation. The interaction of substrates and oligomers with Arthromyces ramosus peroxidase (ARP) was analyzed by docking and molecular dynamics methods. The most possible interaction site of oligomers is the active center of the peroxidase. The affinity of oligomers increases with increasing length of oligomers. However, the complexed oligomers produce non-productive complexes with the peroxidase. Molecular dynamics studies showed that oligomer-peroxidase complexes are stable. It seems likely that strong and stable, but non-productive docking of the oligomers determinates peroxidase inhibition during the reaction by preventing the access of regular substrates to the active center of the enzyme.
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| http://dx.doi.org/10.1016/j.compbiolchem.2004.12.007 | DOI Listing |
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